Q94A52 · RH2_ARATH
- ProteinEukaryotic initiation factor 4A-III homolog
- GeneEIF4A3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids408 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
ATP-dependent RNA helicase. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by MLN51/CASC3, but abolished in presence of the MAGO-Y14 heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGO-Y14 heterodimer increases the RNA-binding affinity of the EJC (By similarity).
Plays a role in abiotic stress adaptation. Can regulate abiotic stress resistance partially via the control of acetoacetyl-CoA thiolase 2 (AC Q8S4Y1) expression (PubMed:26883227).
Plays a role in abiotic stress adaptation. Can regulate abiotic stress resistance partially via the control of acetoacetyl-CoA thiolase 2 (AC Q8S4Y1) expression (PubMed:26883227).
(Microbial infection) Functions as a host RNA helicase that is co-opted by the tombusvirus (TBSV) RNA replication enhancer to greatly enhance tombusvirus replication. Interacts with the viral minus-strand RNA and the replication proteins within the viral replicase.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | exon-exon junction complex | |
Cellular Component | nuclear speck | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | mRNA binding | |
Molecular Function | RNA helicase activity | |
Biological Process | mRNA processing | |
Biological Process | mRNA transport | |
Biological Process | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay | |
Biological Process | regulation of translation | |
Biological Process | response to hypoxia | |
Biological Process | RNA splicing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEukaryotic initiation factor 4A-III homolog
- EC number
- Short namesAteIF4AIII ; eIF-4A-III ; eIF4A-III
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ94A52
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Hypoxia causes transition from diffuse nucleoplasmic localization to accumulation in speckles in nuclei of root cells (PubMed:19435936).
Localized to the nucleus when hypophosphorylated. Hyperphosphorylation of EIF4A3 increases its cytoplasmic localization (PubMed:26887918).
Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (By similarity).
Localized to the nucleus when hypophosphorylated. Hyperphosphorylation of EIF4A3 increases its cytoplasmic localization (PubMed:26887918).
Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions, but mutant seedlings show increased sensitivity to cold and heat stresses.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 100 | Increases cytoplasmic localization; when associated with D-101. | ||||
Sequence: S → D | ||||||
Mutagenesis | 101 | Increases cytoplasmic localization; when associated with D-100. | ||||
Sequence: S → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000239144 | 1-408 | Eukaryotic initiation factor 4A-III homolog | |||
Sequence: MATANPGRGGGRRGGGAMDDDKLVFETTDGIEPITSFNDMGIKEDVLRGVYEYGFEKPSAIQQRAVMPILQGRDVIAQAQSGTGKTSMIALSVCQVVDTSSREVQALILSPTRELATQTEKTIQAIGLHANIQAHACIGGNSVGEDIRKLEHGVHVVSGTPGRVCDMIKRRSLRTRAIKLLILDESDEMLSRGFKDQIYDVYRYLPPDLQVCLVSATLPHEILEMTSKFMTEPVKILVKRDELTLEGIKQFFVAVEKEEWKFDTLCDLYDTLTITQAVIFCNTKRKVDYLSEKMRSHNFTVSSMHGDMPQKERDAIMNEFRSGDSRVLITTDVWARGIDVQQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKSDDIKILRDIEQYYSTQIDEMPMNVADLI | ||||||
Modified residue | 100 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 101 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated at Ser-100 and Ser-101. Phosphorylation status of Ser-100 and Ser-101 largely determines the subcellular localization of EIF4A3.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MATANPGRGGGRRGGGAMDD | ||||||
Motif | 35-63 | Q motif | ||||
Sequence: TSFNDMGIKEDVLRGVYEYGFEKPSAIQQ | ||||||
Domain | 66-236 | Helicase ATP-binding | ||||
Sequence: VMPILQGRDVIAQAQSGTGKTSMIALSVCQVVDTSSREVQALILSPTRELATQTEKTIQAIGLHANIQAHACIGGNSVGEDIRKLEHGVHVVSGTPGRVCDMIKRRSLRTRAIKLLILDESDEMLSRGFKDQIYDVYRYLPPDLQVCLVSATLPHEILEMTSKFMTEPVKI | ||||||
Motif | 184-187 | DEAD box | ||||
Sequence: DESD | ||||||
Domain | 247-408 | Helicase C-terminal | ||||
Sequence: GIKQFFVAVEKEEWKFDTLCDLYDTLTITQAVIFCNTKRKVDYLSEKMRSHNFTVSSMHGDMPQKERDAIMNEFRSGDSRVLITTDVWARGIDVQQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKSDDIKILRDIEQYYSTQIDEMPMNVADLI |
Domain
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence similarities
Belongs to the DEAD box helicase family. DDX48/FAL1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length408
- Mass (Da)45,845
- Last updated2006-05-30 v2
- Checksum4BD11BBA58BAA0D9
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 114 | in Ref. 4; AAK91384/AAN72219 | ||||
Sequence: E → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ010456 EMBL· GenBank· DDBJ | CAA09195.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AP000417 EMBL· GenBank· DDBJ | BAB02563.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
CP002686 EMBL· GenBank· DDBJ | AEE76283.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY050367 EMBL· GenBank· DDBJ | AAK91384.1 EMBL· GenBank· DDBJ | mRNA | ||
BT002207 EMBL· GenBank· DDBJ | AAN72219.1 EMBL· GenBank· DDBJ | mRNA |